SAXSdb — 4j2j

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ataxin-1

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 562–688	Fragment：AXH domain, UNP residues 562-688 Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF)	Protein capicua homolog × 1 （Q96RK0）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 562–688	Fragment：AXH domain, UNP residues 562-688 Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF)	Protein capicua homolog × 1 （Q96RK0）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 562–688	Fragment：AXH domain, UNP residues 562-688 Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF)	Protein capicua homolog × 1 （Q96RK0）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 4J2J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OA8 AXH domain of human spinocerebellar ataxin-1 Deposited 2003-01-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694 Chain B 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；290 K；PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS/HCL, PH 7.0, 0.2M AMMONIUM SULPHATE, 5 MM DTT, 15% PEG 4000, 20% GLYCEROL, AT 290K	Resolution 1.70 Å R-free 0.252
1OA8 AXH domain of human spinocerebellar ataxin-1 Deposited 2003-01-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694 Chain D 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；290 K；PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS/HCL, PH 7.0, 0.2M AMMONIUM SULPHATE, 5 MM DTT, 15% PEG 4000, 20% GLYCEROL, AT 290K	Resolution 1.70 Å R-free 0.252
2M41 Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua Deposited 2013-01-28	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 566–688（123 aa） Fragment：AXH domain, native residues A567-K689	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4APT The structure of the AXH domain of ataxin-1. Deposited 2012-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688 Chain B 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.4 M POTASSIUM SODIUM TARTRATE AT ROOM TEMPERATURE.	Resolution 2.50 Å R-free 0.288
4APT The structure of the AXH domain of ataxin-1. Deposited 2012-04-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688 Chain D 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.4 M POTASSIUM SODIUM TARTRATE AT ROOM TEMPERATURE.	Resolution 2.50 Å R-free 0.288
4AQP The structure of the AXH domain of ataxin-1. Deposited 2012-04-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688 Chain B 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688	Not recorded	NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.1 M MES, PH 6.5, 10% W/V PWG 20000 AT ROOM TEMPERATURE.	Resolution 2.45 Å R-free 0.267
4AQP The structure of the AXH domain of ataxin-1. Deposited 2012-04-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688 Chain D 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.1 M MES, PH 6.5, 10% W/V PWG 20000 AT ROOM TEMPERATURE.	Resolution 2.45 Å R-free 0.267
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ATX1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–129； UniProt 562–688 Author chain B； PDBConstruct 3–129； UniProt 562–688 Author chain C； PDBConstruct 3–129； UniProt 562–688

Protein capicua homolog

Homo sapiens

UniProt Q96RK0

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 28–48	Fragment：UNP residues 28-48	Ataxin-1 × 1 （P54253）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 28–48	Fragment：UNP residues 28-48	Ataxin-1 × 1 （P54253）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 28–48	Fragment：UNP residues 28-48	Ataxin-1 × 1 （P54253）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 4J2J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2M41 Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua Deposited 2013-01-28	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 34–48（15 aa） Fragment：Ataxin-1-binding linear motif (UNP 34-48)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 21–48（28 aa） Fragment：UNP residues 21-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 21–48（28 aa） Fragment：UNP residues 21-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain D 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain G 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain J 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6KZG 14-3-3 protein in Complex with CIC S301 phosphorylated peptide Deposited 2019-09-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 298–305（8 aa） Chain Q 298–305（8 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3350	Resolution 2.00 Å R-free 0.231
6KZH 14-3-3 protein in Complex with CIC S173 phosphorylated peptide Deposited 2019-09-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 170–177（8 aa） Chain Q 170–177（8 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium chloride, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350	Resolution 2.65 Å R-free 0.274
7M5W Crystal structure of the HMG-C1 domain of human capicua bound to DNA Deposited 2021-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 188–280（93 aa） Fragment：HMG box domain UNP residues 188-280 fused with C1 domain UNP residues 1457-1527 Chain A 1457–1527（71 aa） Fragment：HMG box domain UNP residues 188-280 fused with C1 domain UNP residues 1457-1527	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；100 mM MES, 100 mM CaCl2, 100 mM NaCl, and 16% (w/v) PEG 8000	Resolution 2.95 Å R-free 0.243

6 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CIC_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–21； UniProt 28–48 Author chain E； PDBConstruct 1–21； UniProt 28–48 Author chain F； PDBConstruct 1–21； UniProt 28–48

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4j2j
Deposition date deposition_date	2013-02-04
Structure title title	Crystal structure of AXH domain complex with Capicua
Keywords keywords	AXH domain, protein-protein interaction, Capicua, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	26.43 Å
Radius of gyration Rg (electron density) rg_electron	25.53 Å
Forward intensity I(0) i0	33318700.00
Molecular weight molecular_weight	44985.0 kDa
Excluded volume excluded_volume	56358 Å³
Envelope volume envelope_volume	69052 Å³
Hydration-shell volume shell_volume	23856 Å³
Envelope diameter envelope_diameter	91.7 Å
Shell Rg shell_rg	31.14 Å
Envelope Rg envelope_rg	25.85 Å
Shape Rg shape_rg	25.51 Å
Total Rg total_rg	26.25 Å
Total atoms total_atoms	3133
Residues n_residues	392
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	85.3 Å
Rg (real space) rg_real	26.45 Å
Rg uncertainty (real space) rg_real_error	0.71 Å
I(0) (real space) i0_real	3.3320e+07
I(0) uncertainty (real space) i0_real_error	4.6800e+05
Rg (reciprocal space) rg_reciprocal	26.44 Å
I(0) (reciprocal space) i0_reciprocal	33320000.0000
Solution quality estimate total_estimate	0.9046
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.0 Å
Skewness Skewness skewness	0.280
Kurtosis Kurtosis kurtosis	-0.550
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4179000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.984

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Ataxin-1
Molecular weight formula_weight	14296.7 kDa
Mutation mutation	I580M,I605M
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	3161

EFSPAAAPPTLPPYFMKGSMIQLANGELKKVEDLKTEDFIQSAEMSNDLKIDSSTVERIEDSHSPGVAVIQFAVGEHRAQVSVEVLVEYPFFVFGQGWSSCCPERTSQLFDLPCSKLSVGDVCISLTLK

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Protein capicua homolog
Molecular weight formula_weight	2366.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

EPRSVAVFPWHSLVPFLAPSQ

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	28

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d4j2ja_
Class class	b — All beta proteins
Fold Fold fold	b.145 — AXH domain
Superfamily Superfamily superfamily	b.145.1 — AXH domain
Family Family family	b.145.1.1 — AXH domain

Domain ID domain_id	d4j2jb_
Class class	b — All beta proteins
Fold Fold fold	b.145 — AXH domain
Superfamily Superfamily superfamily	b.145.1 — AXH domain
Family Family family	b.145.1.1 — AXH domain

Domain ID domain_id	d4j2jc_
Class class	b — All beta proteins
Fold Fold fold	b.145 — AXH domain
Superfamily Superfamily superfamily	b.145.1 — AXH domain
Family Family family	b.145.1.1 — AXH domain

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8. Citations (1)

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Unit-cell length a length_a	77.722 Å
Unit-cell length b length_b	89.096 Å
Unit-cell length c length_c	132.663 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	43.900 Å
R factor r_factor	0.2230
R_work r_work	0.2230
R_free r_free	0.2700

fit	/app/data/saxs_computation/j2/4j2j/4j2j.fit
pddf	/app/data/pr_computation/j2/4j2j/4j2j.pr.out
profile	/app/data/saxs_computation/j2/4j2j/4j2j.dat

Crystal structure of AXH domain complex with Capicua

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ataxin-1

State in the Current Structure

Other States of the Same Protein in the Database

Protein capicua homolog

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)